7NE9
A single sensor controls large variations in zinc quotas in a marine cyanobacterium
This is a non-PDB format compatible entry.
Summary for 7NE9
| Entry DOI | 10.2210/pdb7ne9/pdb |
| Descriptor | Ferric uptake regulator family, ZINC ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | zinc sensor zur, metallothionein activation, marine cyanobacteria, zinc for co2 fixation, metal binding protein |
| Biological source | Synechococcus sp. (strain WH8102) |
| Total number of polymer chains | 4 |
| Total formula weight | 60070.77 |
| Authors | Fulop, V. (deposition date: 2021-02-03, release date: 2022-03-02, Last modification date: 2024-06-19) |
| Primary citation | Mikhaylina, A.,Ksibe, A.Z.,Wilkinson, R.C.,Smith, D.,Marks, E.,Coverdale, J.P.C.,Fulop, V.,Scanlan, D.J.,Blindauer, C.A. A single sensor controls large variations in zinc quotas in a marine cyanobacterium. Nat.Chem.Biol., 18:869-877, 2022 Cited by PubMed Abstract: Marine cyanobacteria are critical players in global nutrient cycles that crucially depend on trace metals in metalloenzymes, including zinc for CO fixation and phosphorus acquisition. How strains proliferating in the vast oligotrophic ocean gyres thrive at ultra-low zinc concentrations is currently unknown. Using Synechococcus sp. WH8102 as a model we show that its zinc-sensor protein Zur differs from all other known bacterial Zur proteins in overall structure and the location of its sensory zinc site. Uniquely, Synechococcus Zur activates metallothionein gene expression, which supports cellular zinc quotas spanning two orders of magnitude. Thus, a single zinc sensor facilitates growth across pico- to micromolar zinc concentrations with the bonus of banking this precious resource. The resultant ability to grow well at both ultra-low and excess zinc, together with overall lower zinc requirements, likely contribute to the broad ecological distribution of Synechococcus across the global oceans. PubMed: 35681030DOI: 10.1038/s41589-022-01051-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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